ID A0A0N7J878_9BURK Unreviewed; 978 AA.
AC A0A0N7J878;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891};
DE EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891};
DE AltName: Full=Omega-protein {ECO:0000256|ARBA:ARBA00032877};
DE AltName: Full=Relaxing enzyme {ECO:0000256|ARBA:ARBA00032235};
DE AltName: Full=Swivelase {ECO:0000256|ARBA:ARBA00030003};
DE AltName: Full=Untwisting enzyme {ECO:0000256|ARBA:ARBA00031985};
GN Name=topB {ECO:0000313|EMBL:ALK87432.1};
GN ORFNames=L63ED372_00203 {ECO:0000313|EMBL:ALK87432.1};
OS Limnohabitans sp. 63ED37-2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Limnohabitans.
OX NCBI_TaxID=1678128 {ECO:0000313|EMBL:ALK87432.1, ECO:0000313|Proteomes:UP000059510};
RN [1] {ECO:0000313|EMBL:ALK87432.1, ECO:0000313|Proteomes:UP000059510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=63ED37-2 {ECO:0000313|EMBL:ALK87432.1,
RC ECO:0000313|Proteomes:UP000059510};
RA Ahn J.-H., Kim S.B.;
RT "Limnohabitans sp. 2 strains.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC passage and rejoining.; EC=5.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000213};
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00009446}.
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DR EMBL; CP011774; ALK87432.1; -; Genomic_DNA.
DR RefSeq; WP_062402065.1; NZ_CP011774.1.
DR AlphaFoldDB; A0A0N7J878; -.
DR STRING; 1678128.L63ED372_00203; -.
DR KEGG; lih:L63ED372_00203; -.
DR PATRIC; fig|1678128.3.peg.195; -.
DR OrthoDB; 9803554at2; -.
DR Proteomes; UP000059510; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-EC.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd10567; SWIB-MDM2_like; 1.
DR CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR Gene3D; 3.40.50.140; -; 1.
DR Gene3D; 1.10.245.10; SWIB/MDM2 domain; 1.
DR Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
DR Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 1.
DR InterPro; IPR019835; SWIB_domain.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR InterPro; IPR000380; Topo_IA.
DR InterPro; IPR003601; Topo_IA_2.
DR InterPro; IPR023406; Topo_IA_AS.
DR InterPro; IPR013497; Topo_IA_cen.
DR InterPro; IPR013824; Topo_IA_cen_sub1.
DR InterPro; IPR013825; Topo_IA_cen_sub2.
DR InterPro; IPR013826; Topo_IA_cen_sub3.
DR InterPro; IPR023405; Topo_IA_core_domain.
DR InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR InterPro; IPR005738; TopoIII.
DR InterPro; IPR025589; Toprim_C_rpt.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034144; TOPRIM_TopoIII.
DR NCBIfam; TIGR01056; topB; 1.
DR PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1.
DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR Pfam; PF02201; SWIB; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF13342; Toprim_Crpt; 2.
DR PRINTS; PR00417; PRTPISMRASEI.
DR SMART; SM00151; SWIB; 1.
DR SMART; SM00437; TOP1Ac; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR SUPFAM; SSF47592; SWIB/MDM2 domain; 1.
DR PROSITE; PS51925; SWIB_MDM2; 1.
DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ALK87432.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000059510};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 902..978
FT /note="DM2"
FT /evidence="ECO:0000259|PROSITE:PS51925"
FT REGION 846..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 978 AA; 107811 MW; 85066BCBCCD52152 CRC64;
MKTLVIAEKP SVAQDIVKAL TPVAGKFEKH DDHFENDRYV VTSAVGHLVE IQAPEQYDVK
RGKWSFANLP VIPPHFDLKP VDKTKSRLTA VVRQAKRKDV DALINACDAG REGELIFRLI
EQYAGGTKPL NKPVQRLWLQ SMTPQAIRDG FDSLRSNTQM QGLADAARSR SEADWLVGIN
GTRAMTAFNS RDGGFFLTTV GRVQTPTLAV VVEREEQIRK FISRDYWEIH AEFAAAAGTY
PGKWFDPAWK KDEDAEKKAD RKWTAAEAQA IVDAVRGQKA SVSEEATPTT QASPGLFDLT
SLQREANGKF GFSAKTTLAL AQSLYERHKA LTYPRTDSRH LPEDYVPVAK QTFEMLADSG
MRHLAPHALT ALNNNYVRKI PRVFDNKKVS DHFAIIPTLQ APSGLSEAEQ KLYDLVVRRF
MAVFFPSAEY QVTTRISVAA GHSFKTVGKV LVKPGWLAIY GKEAAAEVED AKDGDKGQNL
VPVQAGEQVG VESVEAKGLK TRPPARYSEA TLLGAMEGAG KLVDDDELRE AMQEKGLGTP
ATRAAIIEGL LNEKYMLREG REIIPTAKAF QLMTLLRGLQ VEELSRPELT GEWEYKLAQM
EQGKLSRATF MAEIAAMTEH IVKKAKEYDR DTVPGDYATL STPCPTCGGV VKENYRRYTC
TGADGASDGC GFSFGKSPAG RTFEQVEVEQ FMRDKKIGPL EGFRSKAGWP FVAEMALKYN
EEEKNWKLEF DFGDDKKNEE SGEIVELTDE ALGACPKCGS PVHEHGSNYV CSKAVPTNEQ
PTPSCDFKTG KLILQQPVER EQIVKLLNSG KTDVLDKFVS NRTRRPFKAM LAWNPEEGKV
TFEFEQREGG KKYPPRKTAA TKTPFGKAAA KKTTAKTASK TAKAPAAKKA AKPAAEKAPR
KAAVGTLQPS PALMAVIGDG TYARTEVVKK IWDYIKANNL QDPADKRSIK ADGKLQAVFG
KESATMFELA GIIGKHLS
//
